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June 2, 1987Biochemistry

Adenosine deaminase: viscosity studies and the mechanism of binding of substrate and of ground- and transition-state analog inhibitors

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Population

Adenosine deaminase enzyme system (in vitro)

Design

Preclinical

Authors

LKLinda C. KurzWashington University in St. LouisEWEmma WeitkampUniversity of the West of EnglandCFCarl FriedenWashington University in St. Louis

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Implication

Advances kinetic models of adenosine deaminase; leaves open translation to cardiovascular adenosine signaling.

Structured PICO

P
Population
Adenosine deaminase enzyme system (in vitro)
I
Intervention
Viscosogenic agents (sucrose and ficoll)
O
Outcome
Hydrolysis rates of adenosine and 6-methoxypurine riboside, and rates of association and dissociation of ground-state and transition-state analogue inhibitorssurrogate

The reaction of adenosine deaminase with adenosine is encounter-controlled, as demonstrated by its dependence on microscopic viscosity.

Cite This Study

Kurz et al. (1987) studied this question.

synapsesocial.com/papers/6a1d292b750575be8d2f3cc7https://doi.org/10.1021/bi00385a012
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Also Consider

Synapse has enriched 2 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Influence of substituent ribose on transition state affinity in reactions catalyzed by adenosine deaminase1977 · 54 citations
  2. 2Diffusion-Controlled Macromolecular Interactions1985 · 739 citations